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See detailPurification and characterisation of a 31 kDa chitinase from the Myzus persicae aphid, a target for Hemiptera biocontrol
Francis, Frédéric ULg; Saguez, Julien; Cherqui, Anas et al

in Applied Biochemistry and Biotechnology (2012), 166

Detailed reference viewed: 71 (19 ULg)
See detailPurification and characterisation of phage tail-like bacteriocin induced in Serratia sp.
Jabrane, A.; Vandenberghe, I.; Van beeumen, J. et al

Poster (1997, August)

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See detailPurification and Characterization of a 315 Kda Keratinolytic Subtilisin-Like Serine Protease from Microsporum Canis and Evidence of Its Secretion in Naturally Infected Cats
Mignon, Bernard ULg; Swinnen, M.; Bouchara, J. P. et al

in Medical Mycology (1998), 36(6), 395-404

A keratinolytic protease, secreted as the major component by a feline clinical isolate of Microsporum canis cultivated in a minimal medium containing cat keratin, was purified by affinity chromatography ... [more ▼]

A keratinolytic protease, secreted as the major component by a feline clinical isolate of Microsporum canis cultivated in a minimal medium containing cat keratin, was purified by affinity chromatography on bacitracin agarose and gel filtration. The apparent molecular mass of the enzyme was 31.5 kDa and the pI was 11.8. The enzyme was not glycosylated and its first 15 N-terminal amino acids showed numerous similarities with other fungal subtilisins. The optimum pH was around 9 while inactivation of the enzyme was reversible at pH 4, but not at pH 11. The enzyme was stable at 37 degrees C with an apparent optimum temperature around 55 degrees C. PMSF, soybean trypsin inhibitor (SBTI) and chymostatin strongly inhibited the proteinase. The highest affinity (Km of 0.37 mM) and physiological efficiency (k(cat)/Km) were obtained for the synthetic substrate N-Suc-Ala-Ala-Pro-Phe-p-nitroanilide. These results indicate that the keratinase belongs to the subtilisin-like serine protease family. Purified rabbit immunoglobulins G prepared against the keratinase and used in an immunohistochemical test allowed the detection of the keratinase produced by the fungus invading hair structures in naturally infected cats. The in vitro keratinolytic activity of the enzyme and its production in vivo suggest that it may contribute to pathogenicity. [less ▲]

Detailed reference viewed: 39 (5 ULg)
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See detailPurification and characterization of a 43.5 kDa keratinase from Microsporum canis
Brouta, F.; Descamps, F.; Fett, Thomas ULg et al

Conference (2000)

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See detailPurification and characterization of a 43.5 kDa keratinolytic metalloprotease from Microsporum canis.
Brouta, F.; Descamps, F.; Fett, Thomas ULg et al

in Medical Mycology (2001), 39(3), 269-275

A keratinolytic protease secreted by a feline clinical isolate of Microsporum canis cultivated in a broth containing feline keratin as the sole nitrogen source was purified from the culture filtrate by ... [more ▼]

A keratinolytic protease secreted by a feline clinical isolate of Microsporum canis cultivated in a broth containing feline keratin as the sole nitrogen source was purified from the culture filtrate by affinity chromatography on bacitracin-agarose and by hydrophobic chromatography on octyl-agarose. The enzyme had an apparent molecular mass of 43.5 kDa and the pI was 7.7. It had a significant activity against keratin azure, elastin-Congo red and denatured type I collagen (azocoll). Using the latter substrate, the optimum pH was around 8 and the apparent optimum temperature around 50 degrees C. The protease was strongly inhibited by 1,10-phenanthroline, phosphoramidon and EDTA. The first 13 N-terminal amino acid sequence showed a 61% homology with that of the extracellular metalloprotease of Aspergillus fumigatus and with the neutral protease I of A. oryzae, confirming that this 43.5 kDa keratinase is a metalloprotease. This keratinolytic metalloprotease could be a virulence-related factor involved in pathophysiological mechanisms of M. canis dermatophytosis. [less ▲]

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See detailPurification and characterization of a bovine pregnancy-associated glycoprotein
Zoli, André Pagnah; Beckers, Jean-François ULg; Wouters-Ballman, Patricia et al

in Biology of Reproduction (1991), 45(1), 1-10

A 67000 Mr bovine pregnancy-associated glycoprotein (bPAG) has been isolated from fetal cotyledons and purified to homogeneity by HPLC. The purification was monitored by a double immunodiffusion test and ... [more ▼]

A 67000 Mr bovine pregnancy-associated glycoprotein (bPAG) has been isolated from fetal cotyledons and purified to homogeneity by HPLC. The purification was monitored by a double immunodiffusion test and by RIA in conjunction with an antiserum raised against a crude fraction of placenta-specific antigens. The molecular weight of bPAG was estimated to be 67000 by SDS-PAGE. The isoelectric points (pI) of the four isoforms, determined by high-resolution analytical electrofocusing in polyacrylamide gel, were 4.4, 4.6, 5.2, and 5.4. The carbohydrate content of the bPAG consisted of approximately 10.02 +/- 1.09% neutral sugar and variant amounts of sialic acid (from 0.29 +/- 0.06% in the most basic isoform to 2.1 +/- 0.31% in the most acidic isoform). A specific antiserum was raised against the purified bPAG. A specific RIA showed that the bPAG was antigenically unrelated to BSA, alphafetoprotein (AFP), and human schwangerschafts-spezifischen (pregnancy-specific) beta 1 glycoprotein (SP1). According to some characteristics (e.g. the molecular weight), the purified bPAG may correspond to a form of the pregnancy-specific protein B previously described by Sasser and colleagues (Biol Reprod 1986; 35:936-942). [less ▲]

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See detailPurification and characterization of a carboxylesterase involved in malathion-specific resistance from Tribolium castaneum (Coleoptera: Tenebrionidae).
Amichot, Marcel; Haubruge, Eric ULg; Bergé, Jean-Baptiste et al

in Insect Biochemistry and Molecular Biology (2008), 32

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See detailPurification and characterization of a microbial dehydrogenase - A vanillin : NAD(P)(+) oxidoreductase
Bare, G.; Swiatkowski, T.; Moukil, A. et al

in Applied Biochemistry and Biotechnology (2002), 98-100(Spring), 415-428

Pseudomonas fluorescens (strain BTP9) was found to have at least two NAD(P)-dependent vanillin dehydrogenases: one is induced by vanillin, and the other is constitutive. The constitutive enzyme was ... [more ▼]

Pseudomonas fluorescens (strain BTP9) was found to have at least two NAD(P)-dependent vanillin dehydrogenases: one is induced by vanillin, and the other is constitutive. The constitutive enzyme was purified by ammonium sulfate fractionation, gel-filtration, and Q-Sepharose chromatography. The subunit Mr value was 55,000, determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The native M, value estimated by gel-filtration chromatography gave a value of 210,000. The enzyme made use of NAD(+) less effectively than NADP(+). Benzaldehyde, 4-hydroxybenzaldehyde, hexanal, and acetaldehyde were not oxidized at detectable rates in the presence of NAD(+) or NADP(+). The ultraviolet absorption spectrum indicated that there is no cofactor or prosthetic group bound. The vanillin oxidation reaction was essentially irreversible. The pH optimum was 9.5 and the pI of the enzyme was 4.9. Enzyme activity was not affected when assayed in the presence of salts, except FeCl2. The enzyme was inhibited by the thiol-blocking reagents 4-chloromercuribenzoate and N-ethylmaleimide. NAD(+) and NADP(+) protected the enzyme against such a type of inhibition along with vanillin to a lesser extent. The enzyme exhibited esterase activity with 4-nitrophenyl acetate as substrate and was activated by low concentrations of NAD(+) or NADP(+). We compared the properties of the enzyme with those of some well-characterized microbial benzaldehyde dehydrogenases. [less ▲]

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See detailPurification and characterization of a pregnancy-associated glycoprotein (ovPAG-6) from sheep placenta removed between 66 to 100 days of gestation.
El Amiri, B.; Remy, B.; Melo de Sousa, Noelita ULg et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2002), 6(1), 12-13

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See detailPurification and Characterization of a β-lactam-Resistant Penicillin-Binding Protein from Enterococcus hirae (Streptococcus faecium)
Jacques, Philippe; El Kharroubi, Aboubaker; Joris, Bernard ULg et al

in Actor, Paul; Daneo-Moore, Lolita; Higgins, Michael L. (Eds.) et al Antibiotic Inhibition of Bacterial Cell Surface Assembly and Function (1988)

Detailed reference viewed: 15 (3 ULg)
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See detailPurification and characterization of bovine chorionic somatomammotrophin (bCS)
Beckers, Jean-François ULg; Wouters-Ballman, P; Ectors, F

Conference (1988)

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See detailPurification and characterization of glutathione S-transferases from two syrphid flies (Syrphus ribesii and Myathropa florae).
Vanhaelen, Nicolas; Francis, Frédéric ULg; Haubruge, Eric ULg

in Comparative Biochemistry & Physiology Part B (2004), 137(1), 95-100

Glutathione S-transferases (GST) play an important role in the detoxification of many substances including organic pollutants and plant secondary metabolites. We compared the GST of two syrphid species ... [more ▼]

Glutathione S-transferases (GST) play an important role in the detoxification of many substances including organic pollutants and plant secondary metabolites. We compared the GST of two syrphid species, the aphidophagous Syrphus ribesii and the saprophagous Myathropa florea to assess the relation between feeding type and GST patterns. Differences between the GST of the hoverfly species were observed after purification by affinity chromatography, SDS-PAGE and kinetic studies. While the specific activities of the purified enzymes were different, the purification yields were similar. The variation in specific activities was related to the presence of different isoenzymes in both syrphid species by SDS-PAGE. While two bands of 24 and 32 kDa were observed for M. florea, one more band of 26 kDa was present in S. ribesii. When a range of substrate and glutathione concentrations was tested, differences in Km and Vmax between the glutathione S-transferases from both hoverfly species were also observed. These results are discussed in terms of adaptations to the feeding habit and the habitat of the two syrphid species. [less ▲]

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See detailPurification and Characterization of Pbp4a, a New Low-Molecular-Weight Penicillin-Binding Protein from Bacillus subtilis
Duez, Colette ULg; Vanhove, Marc; Gallet, Xavier et al

in Journal of Bacteriology (2001), 183(5), 1595-9

Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits DD-carboxypeptidase and thiolesterase activities in vitro. Although highly ... [more ▼]

Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits DD-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frere, and J. M. Ghuysen, Biochem. J. 282:781-788, 1992), which is rapidly inactivated by many beta-lactams, PBP4a is only moderately sensitive to these compounds. The second-order rate constant (k(2)/K) for the acylation of the essential serine by benzylpenicillin is 300,000 M(-1) s(-1) for the Actinomadura sp. strain R39 peptidase, 1,400 M(-1) s(-1) for B. subtilis PBP4a, and 7,000 M(-1) s(-1) for Escherichia coli PBP4, the third member of this class of PBPs. Cephaloridine, however, efficiently inactivates PBP4a (k(2)/K = 46,000 M(-1) s(-1)). PBP4a is also much more thermostable than the R39 enzyme. [less ▲]

Detailed reference viewed: 65 (37 ULg)